Amyloid-beta proteins that form cytotoxic aggregates called amyloid-β derived diffusible ligands are responsible for various neurodegenerative diseases like Alzheimer’s and Parkinson’s disease. Novel methods for the early detection of such aggregates and inhibition of further fibrillation are highly important and need in the current situation. In this paper, we present a novel method based on fluorescence resonance energy transfer (FRET) between carbon dots and Ag nanoparticle for sensing various fibrillation stages of beta-amyloid proteins. The addition of Ag nanoparticles to carbon dot colloid is found to significantly enhance the inhibition of beta-amyloid fibrillation due to the modified hydrophobic and electrostatic interactions introduced by Ag nanoparticles and is monitored using thioflavin T (ThT) assay. Further, fluorescence quenching of carbon dots in the presence of Ag particles is found to get reduced with the increase in the incubation time of beta-amyloid fibrils. We could observe a linear trend in the variation of Stern–Volmer constants calculated based on FRET between carbon dots and Ag nanoparticles with the incubation time of beta-amyloid, indicating the potential of using the proposed FRET-based method for sensing beta-amyloid fibrillation.

形成细胞毒性聚集体的淀粉样蛋白-β蛋白（称为淀粉样蛋白-β衍生的可扩散配体）负责各种神经退行性疾病，例如阿尔茨海默氏病和帕金森氏病。早期检测这种聚集体并抑制进一步的原纤维形成的新方法非常重要，在当前情况下是必需的。在本文中，我们提出了一种基于碳点和Ag纳米粒子之间的荧光共振能量转移（FRET）的新方法，用于检测β-淀粉样蛋白的各种原纤维化阶段。已发现将银纳米颗粒添加到碳点胶体中可显着增强对β-淀粉样蛋白原纤维化的抑制，这是由于银纳米颗粒引入了改性的疏水和静电相互作用，并使用硫代黄素T（ThT）测定法进行了监测。进一步，发现在银颗粒存在下碳点的荧光猝灭随着β-淀粉样蛋白原纤维温育时间的增加而减少。我们可以观察到基于FRET计算的碳点和Ag纳米颗粒之间随FRET的Stern-Volmer常数随β-淀粉样蛋白的潜伏时间的线性趋势，这表明使用建议的基于FRET的方法检测β-淀粉样蛋白原纤维化的潜力。